[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=New Zealand white; PubMed=2847925 [NCBI, ExPASy, EBI, Israel, Japan] Pompon D.; "cDNA cloning and functional expression in yeast Saccharomyces cerevisiae of beta-naphthoflavone-induced rabbit liver P-450 LM4 and LM6."; Eur. J. Biochem. 177:285-293(1988).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=3667560 [NCBI, ExPASy, EBI, Israel, Japan] Kagawa N., Mihara K., Sato R.; "Structural analysis of cloned cDNAs for polycyclic hydrocarbon-inducible forms of rabbit liver microsomal cytochrome P-450."; J. Biochem. 101:1471-1479(1987).
[3]	PROTEIN SEQUENCE OF 2-516. PubMed=3949797 [NCBI, ExPASy, EBI, Israel, Japan] Ozols J.; "Complete amino acid sequence of a cytochrome P-450 isolated from beta-naphthoflavone-induced rabbit liver microsomes. Comparison with phenobarbital-induced and constitutive isozymes and identification of invariant residues."; J. Biol. Chem. 261:3965-3979(1986).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 92-515. PubMed=2991917 [NCBI, ExPASy, EBI, Israel, Japan] Okino S.T., Quattrochi L.C., Barnes H.J., Osanto S., Griffin K.J., Johnson E.F., Tukey R.H.; "Cloning and characterization of cDNAs encoding 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible rabbit mRNAs for cytochrome P-450 isozymes 4 and 6."; Proc. Natl. Acad. Sci. U.S.A. 82:5310-5314(1985).
[5]	PROTEIN SEQUENCE OF 176-185. DOI=10.1021/bi00158a019; PubMed=1420171 [NCBI, ExPASy, EBI, Israel, Japan] Yun C.H., Hammons G.J., Jones G., Martin M.V., Hopkins N.E., Alworth W.L., Guengerich F.P.; "Modification of cytochrome P450 1A2 enzymes by the mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl."; Biochemistry 31:10556-10563(1992).
[6]	PARTIAL PROTEIN SEQUENCE. PubMed=6589592 [NCBI, ExPASy, EBI, Israel, Japan] Fujita V.S., Black S.D., Tarr G.E., Koop D.R., Coon M.J.; "On the amino acid sequence of cytochrome P-450 isozyme 4 from rabbit liver microsomes."; Proc. Natl. Acad. Sci. U.S.A. 81:4260-4264(1984).

Comments

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation.
CATALYTIC ACTIVITY: RH + reduced flavoprotein + O₂ = ROH + oxidized flavoprotein + H₂O.
COFACTOR: Heme group (By similarity).
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
INDUCTION: By beta-naphthoflavone and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X13853; CAA32066.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M36538; AAA31437.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05686; CAA29171.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11728; AAA31433.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B27821; O4RBBN.

3D structure databases

HSSP

P00179; 1DT6. [HSSP ENTRY / PDB]

SMR

P00187; 34-514.

ModBase

P00187.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0050381;	Molecular function: unspecific monooxygenase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
IPR008066; Cyt_P450_E_grp-I_CYP1.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.
PTHR19383:SF63; Cyt_P450_E_grp-I_CYP1; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR01683; EP450ICYP1A.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

ProtoNet

P00187.

Genome annotation databases

Ensembl

ENSOCUG00000010056; Oryctolagus cuniculus. [Contig view]

Phylogenomic databases

HOVERGEN

P00187; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 516`	`515`	`Cytochrome P450 1A2.`	`PRO_0000051655`
`REGION`	`361 365`	`5`	`Substrate binding.`
`METAL`	`458 458`		`Iron (heme axial ligand).`
`SITE`	`403 403`	`1`	`Involved in electron transfer with reductase.`
`MOD_RES`	`289 289`		`N6-acetyllysine (By similarity).`
`VARIANT`	`174 174`	`1`	`G -> S.`
`VARIANT`	`233 233`	`1`	`G -> S.`
`VARIANT`	`299 299`	`1`	`S -> G.`
`CONFLICT`	`22 22`		`C -> S (in Ref. 3; AA sequence).`
`CONFLICT`	`67 67`		`R -> P (in Ref. 1; AAA31437).`
`CONFLICT`	`70 70`		`R -> Q (in Ref. 3; AA sequence).`
`CONFLICT`	`92 92`		`D -> N (in Ref. 3 and 4).`
`CONFLICT`	`121 121`		`Q -> H (in Ref. 2; CAA29171).`
`CONFLICT`	`172 172`		`L -> F (in Ref. 3; AA sequence).`
`CONFLICT`	`194 194`		`V -> S (in Ref. 3; AA sequence).`
`CONFLICT`	`208 212`		`RFPQG -> FPQGM (in Ref. 3; AA sequence).`
`CONFLICT`	`208 208`		`R -> H (in Ref. 1; AAA31437).`
`CONFLICT`	`247 251`		`NRPLQ -> QPNLR (in Ref. 3; AA sequence).`
`CONFLICT`	`289 302`		`KHSEKNSKANSGLI -> IKHNEMDSMDDGAHV (in Ref. 4).`
`CONFLICT`	`354 355`		`AR -> PG (in Ref. 1; CAA32066/AAA31437).`
`CONFLICT`	`358 358`		`R -> L (in Ref. 3; AAA31433).`
`CONFLICT`	`359 359`		`L -> I (in Ref. 3 and 4).`
`CONFLICT`	`462 462`		`T -> I (in Ref. 4; AAA31433).`
`CONFLICT`	`494 494`		`I -> T (in Ref. 3 and 4).`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 58334 Da [This is the MW of the unprocessed precursor]

CRC64: 3FD074D74A47C3EF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAMSPAAPLS VTELLLVSAV FCLVFWAVRA SRPKVPKGLK RLPGPWGWPL LGHLLTLGKN 

        70         80         90        100        110        120 
PHVALARLSR RYGDVFQIRL GSTPVVVLSG LDTIKQALVR QGDDFKGRPD LYSSSFITEG 

       130        140        150        160        170        180 
QSMTFSPDSG PVWAARRRLA QDSLKSFSIA SNPASSSSCY LEEHVSQEAE NLIGRFQELM 

       190        200        210        220        230        240 
AAVGRFDPYS QLVVSAARVI GAMCFGRRFP QGSEEMLDVV RNSSKFVETA SSGSPVDFFP 

       250        260        270        280        290        300 
ILRYLPNRPL QRFKDFNQRF LRFLQKTVRE HYEDFDRNSI QDITGALFKH SEKNSKANSG 

       310        320        330        340        350        360 
LIPQEKIVNL VNDIFGAGFD TITTALSWSL MYLVTNPRRQ RKIQEELDAV VGRARQPRLS 

       370        380        390        400        410        420 
DRPQLPYLEA FILELFRHTS FVPFTIPHST TRDTTLNGFH IPKECCIFIN QWQINHDPQL 

       430        440        450        460        470        480 
WGDPEEFRPE RFLTADGAAI NKPLSEKVTL FGLGKRRCIG ETLARWEVFL FLAILLQRLE 

       490        500        510 
FSVPPGVPVD LTPIYGLTMK HPRCEHVQAR PRFSDQ

P00187 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools